Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by preventing interaction with 14-3-3 protein

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by preventing interaction with 14-3-3 protein. / Fuglsang, Anja Thoe; Guo, Yan; Cuin, Tracey A.; Qiu, Quansheng; Song, Chunpeng; Kristiansen, Kim Anker; Bych, Katrine; Schulz, Alexander; Shabala, Sergey; Schumaker, Karen S.; Palmgren, Michael Gjedde; Zhu, Jian-Kang.

In: Plant Cell, Vol. 19, No. 5, 2007, p. 1617-1634.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Fuglsang, AT, Guo, Y, Cuin, TA, Qiu, Q, Song, C, Kristiansen, KA, Bych, K, Schulz, A, Shabala, S, Schumaker, KS, Palmgren, MG & Zhu, J-K 2007, 'Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by preventing interaction with 14-3-3 protein', Plant Cell, vol. 19, no. 5, pp. 1617-1634. https://doi.org/10.1105/tpc.105.035626

APA

Fuglsang, A. T., Guo, Y., Cuin, T. A., Qiu, Q., Song, C., Kristiansen, K. A., Bych, K., Schulz, A., Shabala, S., Schumaker, K. S., Palmgren, M. G., & Zhu, J-K. (2007). Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by preventing interaction with 14-3-3 protein. Plant Cell, 19(5), 1617-1634. https://doi.org/10.1105/tpc.105.035626

Vancouver

Fuglsang AT, Guo Y, Cuin TA, Qiu Q, Song C, Kristiansen KA et al. Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by preventing interaction with 14-3-3 protein. Plant Cell. 2007;19(5):1617-1634. https://doi.org/10.1105/tpc.105.035626

Author

Fuglsang, Anja Thoe ; Guo, Yan ; Cuin, Tracey A. ; Qiu, Quansheng ; Song, Chunpeng ; Kristiansen, Kim Anker ; Bych, Katrine ; Schulz, Alexander ; Shabala, Sergey ; Schumaker, Karen S. ; Palmgren, Michael Gjedde ; Zhu, Jian-Kang. / Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by preventing interaction with 14-3-3 protein. In: Plant Cell. 2007 ; Vol. 19, No. 5. pp. 1617-1634.

Bibtex

@article{6e740ed0a1c211ddb6ae000ea68e967b,
title = "Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by preventing interaction with 14-3-3 protein",
abstract = "Regulation of the trans-plasma membrane pH gradient is an important part of plant responses to several hormonal andenvironmental cues, including auxin, blue light, and fungal elicitors. However, little is known about the signalingcomponents that mediate this regulation. Here, we report that an Arabidopsis thaliana Ser/Thr protein kinase, PKS5, is anegative regulator of the plasma membrane proton pump (PM H{\th}-ATPase). Loss-of-function pks5 mutant plants are moretolerant of high external pH due to extrusion of protons to the extracellular space. PKS5 phosphorylates the PM H{\th}-ATPaseAHA2 at a novel site, Ser-931, in the C-terminal regulatory domain. Phosphorylation at this site inhibits interaction betweenthe PM H{\th}-ATPase and an activating 14-3-3 protein in a yeast expression system. We show that PKS5 interacts with thecalcium binding protein SCaBP1 and that high external pH can trigger an increase in the concentration of cytosolic-freecalcium. These results suggest that PKS5 is part of a calcium-signaling pathway mediating PM H{\th}-ATPase regulation.",
author = "Fuglsang, {Anja Thoe} and Yan Guo and Cuin, {Tracey A.} and Quansheng Qiu and Chunpeng Song and Kristiansen, {Kim Anker} and Katrine Bych and Alexander Schulz and Sergey Shabala and Schumaker, {Karen S.} and Palmgren, {Michael Gjedde} and Jian-Kang Zhu",
year = "2007",
doi = "10.1105/tpc.105.035626",
language = "English",
volume = "19",
pages = "1617--1634",
journal = "The Plant Cell",
issn = "1040-4651",
publisher = "American Society of Plant Biologists",
number = "5",

}

RIS

TY - JOUR

T1 - Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by preventing interaction with 14-3-3 protein

AU - Fuglsang, Anja Thoe

AU - Guo, Yan

AU - Cuin, Tracey A.

AU - Qiu, Quansheng

AU - Song, Chunpeng

AU - Kristiansen, Kim Anker

AU - Bych, Katrine

AU - Schulz, Alexander

AU - Shabala, Sergey

AU - Schumaker, Karen S.

AU - Palmgren, Michael Gjedde

AU - Zhu, Jian-Kang

PY - 2007

Y1 - 2007

N2 - Regulation of the trans-plasma membrane pH gradient is an important part of plant responses to several hormonal andenvironmental cues, including auxin, blue light, and fungal elicitors. However, little is known about the signalingcomponents that mediate this regulation. Here, we report that an Arabidopsis thaliana Ser/Thr protein kinase, PKS5, is anegative regulator of the plasma membrane proton pump (PM Hþ-ATPase). Loss-of-function pks5 mutant plants are moretolerant of high external pH due to extrusion of protons to the extracellular space. PKS5 phosphorylates the PM Hþ-ATPaseAHA2 at a novel site, Ser-931, in the C-terminal regulatory domain. Phosphorylation at this site inhibits interaction betweenthe PM Hþ-ATPase and an activating 14-3-3 protein in a yeast expression system. We show that PKS5 interacts with thecalcium binding protein SCaBP1 and that high external pH can trigger an increase in the concentration of cytosolic-freecalcium. These results suggest that PKS5 is part of a calcium-signaling pathway mediating PM Hþ-ATPase regulation.

AB - Regulation of the trans-plasma membrane pH gradient is an important part of plant responses to several hormonal andenvironmental cues, including auxin, blue light, and fungal elicitors. However, little is known about the signalingcomponents that mediate this regulation. Here, we report that an Arabidopsis thaliana Ser/Thr protein kinase, PKS5, is anegative regulator of the plasma membrane proton pump (PM Hþ-ATPase). Loss-of-function pks5 mutant plants are moretolerant of high external pH due to extrusion of protons to the extracellular space. PKS5 phosphorylates the PM Hþ-ATPaseAHA2 at a novel site, Ser-931, in the C-terminal regulatory domain. Phosphorylation at this site inhibits interaction betweenthe PM Hþ-ATPase and an activating 14-3-3 protein in a yeast expression system. We show that PKS5 interacts with thecalcium binding protein SCaBP1 and that high external pH can trigger an increase in the concentration of cytosolic-freecalcium. These results suggest that PKS5 is part of a calcium-signaling pathway mediating PM Hþ-ATPase regulation.

U2 - 10.1105/tpc.105.035626

DO - 10.1105/tpc.105.035626

M3 - Journal article

C2 - 17483306

VL - 19

SP - 1617

EP - 1634

JO - The Plant Cell

JF - The Plant Cell

SN - 1040-4651

IS - 5

ER -

ID: 8071155